Back
Leucine-rich nuclear-export signals: born to be weak.
Journal article

Leucine-rich nuclear-export signals: born to be weak.

  • Kutay U Swiss Federal Institute of Technology (ETH) Zürich, Institute of Biochemistry, Schafmattstrasse 18, HPM F11.1, 8093 Zürich, Switzerland. ulrike.kutay@bc.biol.ethz.ch
  • Güttinger S
  • 2005-03-09
Published in:
  • Trends in cell biology. - 2005
Active Transport, Cell Nucleus
Amino Acid Sequence
Animals
Binding Sites
Cell Nucleus
Cytoplasm
Humans
Karyopherins
Leucine
Models, Biological
Molecular Sequence Data
Nuclear Pore
Receptors, Cytoplasmic and Nuclear
Sequence Homology, Amino Acid
Signal Transduction
English CRM1 mediates the nuclear export of proteins exposing leucine-rich nuclear-export signals (NESs). Most NESs bind to CRM1 with relatively low affinity. Recently, higher-affinity NESs were selected from a 15-mer random peptide library. Unexpectedly, complexes between high-affinity NESs and CRM1 accumulate at the cytoplasmic filaments of the nuclear pore complex (NPC). This finding suggests that high-affinity NES binding to CRM1 impairs the efficient release of export complexes from the NPC, explaining why leucine-rich NESs have evolved to be weak.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/228283
Statistics
Document views: 29 File downloads: